Essential hyaluronan structure for binding with hyaluronan-binding protein (HABP) determined by glycotechnological approach

Carbohydr Polym. 2021 Jan 1;251:116989. doi: 10.1016/j.carbpol.2020.116989. Epub 2020 Aug 30.


Hyaluronan specifically binds to aggrecan globular domain 1, which is often referred to as just hyaluronan binding protein (HABP), however, the hyaluronan carbohydrate structure recognized by HABP had not been studied in detail. The aim of the present study was to investigate the important structure of hyaluronan for binding to HABP. We prepared hybrid oligosaccharides from hyaluronan and chondroitin, with or without modification of the reducing or non-reducing terminus, as tools to determine the preferred structure of hyaluronan for binding to the HABP by a competitive ELISA-like method. The non-reducing terminal structure was critical, especially, the glucuronic acid (GlcUA) and N-acetylglucosamine (GlcNAc) of the hyaluronan-unit are essential for complete HABP binding activity, and for any HABP binding activity, respectively. It is possible to replace GlcUAβ-1-3GlcNAc of the internal disaccharide units with GlcUAβ-1-3N-acetylgalactosamine (GalNAc), if the chain length is decasaccharide or larger.

Keywords: Chondroitin; Glycotechnology; Hyaluronan; Hyaluronan-binding protein; Hyaluronidase.

MeSH terms

  • Aggrecans / chemistry
  • Aggrecans / metabolism
  • Animals
  • Binding Sites
  • Carbohydrate Sequence
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / metabolism
  • Chondroitin / chemistry
  • Chondroitin / metabolism
  • Glycosylation
  • Humans
  • Hyaluronan Receptors / chemistry*
  • Hyaluronan Receptors / metabolism*
  • Hyaluronic Acid / chemistry*
  • Hyaluronic Acid / metabolism*
  • Oligosaccharides / chemistry
  • Oligosaccharides / metabolism
  • Protein Binding


  • Aggrecans
  • Cell Adhesion Molecules
  • Hyaluronan Receptors
  • Oligosaccharides
  • Hyaluronic Acid
  • Chondroitin